ID A0A2J6LE64_LACSA Unreviewed; 165 AA.
AC A0A2J6LE64;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Non-specific lipid-transfer protein {ECO:0000256|RuleBase:RU000628};
GN ORFNames=LSAT_8X108081 {ECO:0000313|EMBL:PLY85617.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY85617.1};
RN [1] {ECO:0000313|EMBL:PLY85617.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
CC -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC phospholipids as well as galactolipids across membranes. May play a
CC role in wax or cutin deposition in the cell walls of expanding
CC epidermal cells and certain secretory tissues.
CC {ECO:0000256|RuleBase:RU000628}.
CC -!- SIMILARITY: Belongs to the plant LTP family.
CC {ECO:0000256|ARBA:ARBA00009748, ECO:0000256|RuleBase:RU000628}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLY85617.1}.
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DR EMBL; NBSK01004225; PLY85617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6LE64; -.
DR STRING; 4236.A0A2J6LE64; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_8X108081_mrna; cds-PLY85617.1; gene-LSAT_8X108081.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_8X108081_mrna; cds-PLY85617.1; gene-LSAT_8X108081.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR CDD; cd01960; nsLTP1; 1.
DR Gene3D; 1.10.110.10; Plant lipid-transfer and hydrophobic proteins; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33076:SF188; NON-SPECIFIC LIPID-TRANSFER PROTEIN; 1.
DR PANTHER; PTHR33076; NON-SPECIFIC LIPID-TRANSFER PROTEIN 2-RELATED; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|RuleBase:RU000628};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|RuleBase:RU000628}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..165
FT /note="Non-specific lipid-transfer protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014344793"
FT DOMAIN 35..119
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical"
FT /evidence="ECO:0000259|SMART:SM00499"
FT REGION 134..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 165 AA; 17704 MW; ED49020B3952B28F CRC64;
MARGEMVRKV ALMVVVVFYC LVVQPPRAVE GQLSCPLVVT SLLPCATYLT SGGPVSRHCC
SGVRSLQSAA TTTDDRQTAC QCMEEAAAML PGINIYNARS LPAKCDVDVS YDINPDTDCS
KVGLYPFGVL ARDPDSAEVQ QQQQRQHDSI NVGSHASKSD CLHNG
//
